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ARTICLE, Cellular/Molecular

Ultrastructural Distribution of the α7 Nicotinic Acetylcholine Receptor Subunit in Rat Hippocampus

Ruth Fabian-Fine, Paul Skehel, Mick L. Errington, Heather A. Davies, Emanuele Sher, Michael G. Stewart and Alan Fine
Journal of Neuroscience 15 October 2001, 21 (20) 7993-8003; DOI: https://doi.org/10.1523/JNEUROSCI.21-20-07993.2001
Ruth Fabian-Fine
1Department of Biological Sciences, The Open University, Milton Keynes, MK7 6AA, United Kingdom,
2Division of Neurophysiology, National Institute for Medical Research, Mill Hill, London NW7 1AA, United Kingdom,
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Paul Skehel
2Division of Neurophysiology, National Institute for Medical Research, Mill Hill, London NW7 1AA, United Kingdom,
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Mick L. Errington
2Division of Neurophysiology, National Institute for Medical Research, Mill Hill, London NW7 1AA, United Kingdom,
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Heather A. Davies
1Department of Biological Sciences, The Open University, Milton Keynes, MK7 6AA, United Kingdom,
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Emanuele Sher
3Lilly Research Centre, Eli Lilly and Co., Erl Wood Manor, Windlesham, Surrey GU20 6PH, United Kingdom, and
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Michael G. Stewart
1Department of Biological Sciences, The Open University, Milton Keynes, MK7 6AA, United Kingdom,
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Alan Fine
2Division of Neurophysiology, National Institute for Medical Research, Mill Hill, London NW7 1AA, United Kingdom,
4Department of Physiology and Biophysics, Dalhousie University Faculty of Medicine, Halifax, Nova Scotia B3H 4H7, Canada
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Abstract

Acetylcholine (ACh) is an important neurotransmitter in the mammalian brain; it is implicated in arousal, learning, and other cognitive functions. Recent studies indicate that nicotinic receptors contribute to these cholinergic effects, in addition to the established role of muscarinic receptors. In the hippocampus, where cholinergic involvement in learning and memory is particularly well documented, α7 nicotinic acetylcholine receptor subunits (α7 nAChRs) are highly expressed, but their precise ultrastructural localization has not been determined. Here, we describe the results of immunogold labeling of serial ultrathin sections through stratum radiatum of area CA1 in the rat. Using both anti-α7 nAChR immunolabeling and α-bungarotoxin binding, we find that α7 nAChRs are present at nearly all synapses in CA1 stratum radiatum, with immunolabeling present at both presynaptic and postsynaptic elements. Morphological considerations and double immunolabeling indicate that GABAergic as well as glutamatergic synapses bear α7 nAChRs, at densities approaching those observed for glutamate receptors in CA1 stratum radiatum. Postsynaptically, α7 nAChRs often are distributed at dendritic spines in a perisynaptic annulus. In the postsynaptic cytoplasm, immunolabeling is associated with spine apparatus and other membranous structures, suggesting that α7 nAChRs may undergo dynamic regulation, with insertion into the synapse and subsequent internalization. The widespread and substantial expression of α7 nAChRs at synapses in the hippocampus is consistent with an important role in mediating and/or modulating synaptic transmission, plasticity, and neurodegeneration.

  • acetylcholine receptors
  • nicotine
  • dendritic spines
  • postsynaptic density
  • immuno-electron microscopy
  • glutamate
  • GABA
  • Aβ1–42
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The Journal of Neuroscience: 21 (20)
Journal of Neuroscience
Vol. 21, Issue 20
15 Oct 2001
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Ultrastructural Distribution of the α7 Nicotinic Acetylcholine Receptor Subunit in Rat Hippocampus
Ruth Fabian-Fine, Paul Skehel, Mick L. Errington, Heather A. Davies, Emanuele Sher, Michael G. Stewart, Alan Fine
Journal of Neuroscience 15 October 2001, 21 (20) 7993-8003; DOI: 10.1523/JNEUROSCI.21-20-07993.2001

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Ultrastructural Distribution of the α7 Nicotinic Acetylcholine Receptor Subunit in Rat Hippocampus
Ruth Fabian-Fine, Paul Skehel, Mick L. Errington, Heather A. Davies, Emanuele Sher, Michael G. Stewart, Alan Fine
Journal of Neuroscience 15 October 2001, 21 (20) 7993-8003; DOI: 10.1523/JNEUROSCI.21-20-07993.2001
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Keywords

  • acetylcholine receptors
  • nicotine
  • dendritic spines
  • postsynaptic density
  • immuno-electron microscopy
  • glutamate
  • GABA
  • Aβ1–42

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